Q0RBM4
Gene name |
proS |
Protein name |
Proline--tRNA ligase |
Names |
Prolyl-tRNA synthetase, ProRS |
Species |
Frankia alni (strain ACN14a) |
KEGG Pathway |
fal:FRAAL6537 |
EC number |
6.1.1.15: Ligases forming aminoacyl-tRNA and related compounds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q0RBM4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0RBM4-F1 | Predicted | AlphaFoldDB |
No variants for Q0RBM4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0RBM4 | |||||
No associated diseases with Q0RBM4
5 regional properties for Q0RBM4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 100 - 258 | IPR002314 |
| domain | Anticodon-binding | 287 - 377 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 31 - 280 | IPR006195 |
| domain | Proline-tRNA ligase, class II, C-terminal | 406 - 468 | IPR016061 |
| domain | Prolyl-tRNA synthetase, catalytic domain | 10 - 269 | IPR033721 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.15 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| proline-tRNA ligase activity | Catalysis of the reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| prolyl-tRNA aminoacylation | The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAVLTSRATD | FPRWYQDVLA | KAELADNGPV | RGTMVIRPYG | YAIWERMQAD | VDARIKAAGA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VNAYFPLFIP | ESYLRREAEH | VEGFSPELAV | VTIGGGKELE | EPVVVRPTSE | TIIGEYLAKW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TQSYRDLPLL | LNQWANVVRW | ELRPRLFLRS | SEFLWQEGHT | AHVDEAEAAA | YARRIALEVY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RDFLTDVLAI | PVFIGTKTRK | ERFAGATNTM | TCEGMMGDGK | ALQMATSHEL | GQNFARAFDI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DFLGADGAKH | LAWTTSWGSS | TRMVGGLIMA | HGDDNGLRIP | PRLAPTQVVV | LPVRDDETVV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AKAREIAAAL | TDAGLRVQVD | ARSGLSFGRR | VTDAEIKGIP | VRVEVGPRDL | AAGNVTLVRR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DTSVKAAVPL | AEAAARVPAL | LDEVQAGLHA | EALALRESRT | ADVTTVADAA | AAAQTGFARI |
| 430 | 440 | 450 | 460 | ||
| PWRLVGEEGE | ARLAEDALTV | RCLQTPDGEI | PPAGGDPDDL | ICLIARSY |